This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Proteins from the BAR domain superfamily [1], ubiquitous in many organisms and cell types (http://www.ks.uiuc.edu/Research/BAR-domain), are implicated in a multitude of cellular processes involving membrane remodeling, e.g., endocytosis, apoptosis, and cell-cell fusion. In vitro, these proteins sculpt high-curvature membrane tubes and vesicles [2, 3] from low-curvature liposomes. BAR domains form banana-shaped homodimers bearing a high density of positively charged residues on the concave surface [4[unreadable]6], which facilitates sculpting of negatively charged membranes. However, single BAR domains induce only local membrane curvature [7, 8], while recent cryo-EM reconstructions [3] reveal that sculpting of membrane tubes and vesicles is performed by many BAR domains arranged in lattice-like scaffolds.